Purification and functional characterization of factor I.

Sara Nilsson; Anna Blom

doi:10.1007/978-1-62703-724-2_15

Purification and functional characterization of factor I.

Sara Nilsson, Anna Blom

Protein Chemistry, Malmö

Research output: Contribution to journal › Article › peer-review

Abstract

Factor I (FI) is a soluble, 88 kDa glycoprotein present in plasma at a concentration of approximately 35 mg/L. FI inhibits all complement pathways as it degrades activated C4b and C3b when these are bound to a cofactor such as C4b-binding protein or factor H. Here, we describe a method for purification of FI from human plasma, which is based on affinity chromatography followed by anion exchange chromatography. We also describe a functional assay, in which activity of FI can be assessed.

Original language	English
Pages (from-to)	177-188
Journal	Methods in Molecular Biology
Volume	1100
DOIs	https://doi.org/10.1007/978-1-62703-724-2_15
Publication status	Published - 2014

Subject classification (UKÄ)

Other Basic Medicine

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10.1007/978-1-62703-724-2_15

http://www.ncbi.nlm.nih.gov/pubmed/24218260?dopt=Abstract

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title = "Purification and functional characterization of factor I.",

abstract = "Factor I (FI) is a soluble, 88 kDa glycoprotein present in plasma at a concentration of approximately 35 mg/L. FI inhibits all complement pathways as it degrades activated C4b and C3b when these are bound to a cofactor such as C4b-binding protein or factor H. Here, we describe a method for purification of FI from human plasma, which is based on affinity chromatography followed by anion exchange chromatography. We also describe a functional assay, in which activity of FI can be assessed.",

author = "Sara Nilsson and Anna Blom",

year = "2014",

doi = "10.1007/978-1-62703-724-2_15",

language = "English",

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journal = "Methods in Molecular Biology",

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AU - Nilsson, Sara

AU - Blom, Anna

PY - 2014

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N2 - Factor I (FI) is a soluble, 88 kDa glycoprotein present in plasma at a concentration of approximately 35 mg/L. FI inhibits all complement pathways as it degrades activated C4b and C3b when these are bound to a cofactor such as C4b-binding protein or factor H. Here, we describe a method for purification of FI from human plasma, which is based on affinity chromatography followed by anion exchange chromatography. We also describe a functional assay, in which activity of FI can be assessed.

AB - Factor I (FI) is a soluble, 88 kDa glycoprotein present in plasma at a concentration of approximately 35 mg/L. FI inhibits all complement pathways as it degrades activated C4b and C3b when these are bound to a cofactor such as C4b-binding protein or factor H. Here, we describe a method for purification of FI from human plasma, which is based on affinity chromatography followed by anion exchange chromatography. We also describe a functional assay, in which activity of FI can be assessed.

U2 - 10.1007/978-1-62703-724-2_15

DO - 10.1007/978-1-62703-724-2_15

M3 - Article

C2 - 24218260

SN - 1940-6029

VL - 1100

SP - 177

EP - 188

JO - Methods in Molecular Biology

JF - Methods in Molecular Biology

ER -

Purification and functional characterization of factor I.

Abstract

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